A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease

Literature Information

Publication Date 2010-08-16
DOI 10.1039/C003568H
Impact Factor 3.676
Authors

Maksim Kouza, S. Gowtham, Max Seel, Ulrich H. E. Hansmann


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Abstract

We study in silico possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease. Our results indicate that the mutation does not have appreciable affects on the stability of copper-bound states but rather destabilizes the characteristic end-to-end β-sheet. In this way, the mutation presumably increases the probability for aggregation and/or degradation leading to decreased concentration of the monomer.

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Physical Chemistry Chemical Physics

Physical Chemistry Chemical Physics
CiteScore: 5.5
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